In this study, the some kinetic and biochemical properties of trypsin enzyme from common kilka and porcine were assessed. The results showed that the optimum temperature and pH for common kilka trypsin and porcine trypsin were 60 °C and 8, respectively. Thermal and pH stability were also 45 °C and 7-10 for common kilka trypsin and 50 °C and 4-11 for porcine trypsin. CaCl2 and MgCl2 significantly increased the trypsin activity in common kilka and porcine (p < 0.05). NaCl and KCl had no significant effect on trysin activity in common kilka (p > 0.05) while it was significantly decreased in porcine in presence of them (p < 0.05). The trypsin activity in common kilka was significantly increased in presence of MnCl2 (p < 0.05) but in porcine, showed a significant decrease (p < 0.05). The comparison of inhibitors of SBTI, TLCK, PMSF and p-aminobenzamidine revealed the except for p-aminobenzamidine, the other inhibitors showed no significant difference on enzyme activity in common kilka and porcine (p > 0.05) but enzyme activity was significantly decreased by p-aminobenzamidine in porcine than common kilka (p < 0.05). Vmax value of common kilka trypsin was significantly higher than that from porcine trypsin (p < 0.05). Km value of common kilka trypsin was significantly lower than that from porcine trypsin (p < 0.05). The results of this study showed that common kilka trypsin was more efficient that porcine trypsin and it could be considered as an additive in industries and biotechnological researches in future.